4ADE
Structural and functional study of succinyl-ornithine transaminase from E. coli
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-04-12 |
| Detector | ADSC QUANTUM 315 |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 231.469, 231.469, 110.416 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 115.730 - 2.750 |
| R-factor | 0.15633 |
| Rwork | 0.154 |
| R-free | 0.20133 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2pb2 |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.803 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.900 | 2.900 |
| High resolution limit [Å] | 2.750 | 2.750 |
| Rmerge | 0.150 | 0.720 |
| Number of reflections | 29220 | |
| <I/σ(I)> | 21.9 | 6 |
| Completeness [%] | 99.3 | 99.2 |
| Redundancy | 22.1 | 22.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5 | 293 | 1.4 M SODIUM MALONATE PH 7, 10% (V/V) MMT (MALATE-MES-TRIS) BUFFER AT PH 5.0, AT 293K WITH A PROTEIN TO CRYSTALLANT RATIO OF 3:1 IN THE PRESENCE OF SILVER BULLET SCREEN NUMBER 62. |
